Characterization of the Amino-terminal Transcriptional Activation Function of the Human Estrogen Receptor in Animal and Yeast Cells

@article{citeulike:2327905, abstract = {We have previously reported that the transcriptional activation function AF-1, located in the A/B region of the human estrogen receptor, exhibits cell-type and promoter context specificity in both animal cells and yeast. To further characterize AF-1, we have constructed a number of deletion mutants spanning the A/B region in the context of either the whole human estrogen receptor or the A/B region linked to the GAL4 DNA binding domain, and tested their transcriptional activity in chicken embryo fibroblasts and in yeast cells, two cell types in which AF-1 efficiently activates transcription on its own. Additionally, we utilized HeLa cells in which AF-1 is poorly active but can synergize with the transcriptional activation function AF-2 located in the hormone binding domain. We show that in animal cells the ``independent'' activity of AF-1 is embodied in a rather hydrophobic proline-rich 99-amino acid activating domain (amino acids 51-149), whereas amino acids 51-93 and 102-149 can independently synergize with AF-2. Interestingly, in yeast, three discrete activating domains (amino acids 1-62, 80-113, and 118-149) are almost as active on their own as the whole A/B region, indicating that multiple activating domains can operate independently in yeast. Our study also demonstrates that, within the context of the whole human estrogen receptor, the same AF-1 activating domains are ``induced'' by either estradiol or 4-hydroxytamoxifen. 10.1074/jbc.270.16.9535}, author = {Metzger, Daniel and Ali, Simak and Bornert, Jean-Marc and Chambon, Pierre }, citeulike-article-id = {2327905}, doi = {10.1074/jbc.270.16.9535}, journal = {J. Biol. Chem.}, month = {April}, number = {16}, pages = {9535--9542}, posted-at = {2008-02-04 02:09:35}, priority = {2}, title = {Characterization of the Amino-terminal Transcriptional Activation Function of the Human Estrogen Receptor in Animal and Yeast Cells}, url = {http://dx.doi.org/10.1074/jbc.270.16.9535}, volume = {270}, year = {1995} }

TY - JOUR ID - citeulike:2327905 L3 - citeulike-article-id:2327905 TI - Characterization of the Amino-terminal Transcriptional Activation Function of the Human Estrogen Receptor in Animal and Yeast Cells JF - J. Biol. Chem. VL - 270 IS - 16 SP - 9535 EP - 9542 N2 - We have previously reported that the transcriptional activation function AF-1, located in the A/B region of the human estrogen receptor, exhibits cell-type and promoter context specificity in both animal cells and yeast. To further characterize AF-1, we have constructed a number of deletion mutants spanning the A/B region in the context of either the whole human estrogen receptor or the A/B region linked to the GAL4 DNA binding domain, and tested their transcriptional activity in chicken embryo fibroblasts and in yeast cells, two cell types in which AF-1 efficiently activates transcription on its own. Additionally, we utilized HeLa cells in which AF-1 is poorly active but can synergize with the transcriptional activation function AF-2 located in the hormone binding domain. We show that in animal cells the ``independent'' activity of AF-1 is embodied in a rather hydrophobic proline-rich 99-amino acid activating domain (amino acids 51-149), whereas amino acids 51-93 and 102-149 can independently synergize with AF-2. Interestingly, in yeast, three discrete activating domains (amino acids 1-62, 80-113, and 118-149) are almost as active on their own as the whole A/B region, indicating that multiple activating domains can operate independently in yeast. Our study also demonstrates that, within the context of the whole human estrogen receptor, the same AF-1 activating domains are ``induced'' by either estradiol or 4-hydroxytamoxifen. 10.1074/jbc.270.16.9535 AU - Metzger, Daniel AU - Ali, Simak AU - Bornert, Jean-Marc AU - Chambon, Pierre PY - 1995/04/21/ UR - http://dx.doi.org/10.1074/jbc.270.16.9535 ER -